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| | {{STRUCTURE_2bol| PDB=2bol | SCENE= }} | | {{STRUCTURE_2bol| PDB=2bol | SCENE= }} |
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| - | '''CRYSTAL STRUCTURE AND ASSEMBLY OF TSP36, A METAZOAN SMALL HEAT SHOCK PROTEIN'''
| + | ===CRYSTAL STRUCTURE AND ASSEMBLY OF TSP36, A METAZOAN SMALL HEAT SHOCK PROTEIN=== |
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| - | ==Overview==
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| - | Small heat shock proteins (sHsps) are oligomers that perform a protective function by binding denatured proteins. Although ubiquitous, they are of variable sequence except for a C-terminal approximately 90-residue "alpha-crystallin domain". Unlike larger stress response chaperones, sHsps are ATP-independent and generally form polydisperse assemblies. One proposed mechanism of action involves these assemblies breaking into smaller subunits in response to stress, before binding unfolding substrate and reforming into larger complexes. Two previously solved non-metazoan sHsp multimers are built from dimers formed by domain swapping between the alpha-crystallin domains, adding to evidence that the smaller subunits are dimers. Here, the 2.5A resolution structure of an sHsp from the parasitic flatworm Taenia saginata Tsp36, the first metazoan crystal structure, shows a new mode of dimerization involving N-terminal regions, which differs from that seen for non-metazoan sHsps. Sequence differences in the alpha-crystallin domains between metazoans and non-metazoans are critical to the different mechanism of dimerization, suggesting that some structural features seen for Tsp36 may be generalized to other metazoan sHsps. The structure also indicates scope for flexible assembly of subunits, supporting the proposed process of oligomer breakdown, substrate binding and reassembly as the chaperone mechanism. It further shows how sHsps can bind coil and secondary structural elements by wrapping them around the alpha-crystallin domain. The structure also illustrates possible roles for conserved residues associated with disease, and suggests a mechanism for the sHsp-related pathogenicity of some flatworm infections. Tsp36, like other flatworm sHsps, possesses two divergent sHsp repeats per monomer. Together with the two previously solved structures, a total of four alpha-crystallin domain structures are now available, giving a better definition of domain boundaries for sHsps.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_16165157}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 16165157 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_16165157}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Small heat shock protein]] | | [[Category: Small heat shock protein]] |
| | [[Category: Taenia saginata]] | | [[Category: Taenia saginata]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 20:34:47 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 15:27:46 2008'' |
Revision as of 12:27, 27 July 2008
Template:STRUCTURE 2bol
CRYSTAL STRUCTURE AND ASSEMBLY OF TSP36, A METAZOAN SMALL HEAT SHOCK PROTEIN
Template:ABSTRACT PUBMED 16165157
About this Structure
2BOL is a Single protein structure of sequence from Taenia saginata. Full crystallographic information is available from OCA.
Reference
Wrapping the alpha-crystallin domain fold in a chaperone assembly., Stamler R, Kappe G, Boelens W, Slingsby C, J Mol Biol. 2005 Oct 14;353(1):68-79. PMID:16165157
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